Myosin chaperones.

Myosin chaperones.
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DOI:
10.1016/j.sbi.2013.11.002
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发表时间:
2014-04
影响因子:
6.8
通讯作者:
Clausen T
Clausen T
中科院分区:
生物学2区
文献类型:
--
作者:
Hellerschmied D;Clausen T

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UCS蛋白质包括不同的肌球蛋白伴侣蛋白家族。UCS分子伴侣在其底物靶向、折叠和活化机制方面不同。无TPR的UCS分子伴侣二聚化以控制肌球蛋白-肌动蛋白相互作用。含有TPR的UCS蛋白组成肌丝的多聚体装配线。UCS活性的失调与包括心脏病在内的肌病有关。肌球蛋白马达蛋白的折叠和组装对于细胞水平上的大多数运动过程以及生物体水平上的运动过程是必不可少的。重要的是,肌球蛋白,这代表了一个非常多样化的蛋白质家族,需要一般和专门的折叠因子的活动,以发展其完整的运动功能。肌球蛋白特异性UCS(UCS-45/Cro 1/She 4)分子伴侣的活性范围从协助肌动蛋白-肌球蛋白依赖性转运过程到支架多亚基分子伴侣复合物,其是组装肌丝所需的。最近的结构-功能研究揭示了含有TPR(tetratricopeptide repeat)和不含TPR的UCS分子伴侣的结构组织。所观察到的结构差异似乎反映了专门的和显着通用的肌球蛋白指导分子伴侣的工作机制,将在本次审查中讨论。
UCS proteins comprise a diverse family of myosin chaperones. UCS chaperones differ in their substrate targeting, folding and activation mechanism. TPR-less UCS chaperones dimerize to control the myosin–actin interaction. TPR-containing UCS proteins compose multimeric assembly lines for myofilaments. Misregulation of UCS activity is linked to myopathies including heart diseases. The folding and assembly of myosin motor proteins is essential for most movement processes at the cellular, but also at the organism level. Importantly, myosins, which represent a very diverse family of proteins, require the activity of general and specialized folding factors to develop their full motor function. The activities of the myosin-specific UCS (UNC-45/Cro1/She4) chaperones range from assisting acto-myosin dependent transport processes to scaffolding multi-subunit chaperone complexes, which are required to assemble myofilaments. Recent structure–function studies revealed the structural organization of TPR (tetratricopeptide repeat)-containing and TPR-less UCS chaperones. The observed structural differences seem to reflect the specialized and remarkably versatile working mechanisms of myosin-directed chaperones, as will be discussed in this review.
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